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Database: UniProt
Entry: V2XCL3_MONRO
LinkDB: V2XCL3_MONRO
Original site: V2XCL3_MONRO 
ID   V2XCL3_MONRO            Unreviewed;       553 AA.
AC   V2XCL3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   08-NOV-2023, entry version 42.
DE   SubName: Full=Meiosis-specific apc c activator protein ama1 {ECO:0000313|EMBL:ESK91457.1};
GN   ORFNames=Moror_2681 {ECO:0000313|EMBL:ESK91457.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK91457.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK91457.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK91457.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
CC   -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family.
CC       {ECO:0000256|ARBA:ARBA00006445}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESK91457.1}.
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DR   EMBL; AWSO01000345; ESK91457.1; -; Genomic_DNA.
DR   RefSeq; XP_007849248.1; XM_007851057.1.
DR   AlphaFoldDB; V2XCL3; -.
DR   STRING; 1381753.V2XCL3; -.
DR   KEGG; mrr:Moror_2681; -.
DR   HOGENOM; CLU_014831_4_2_1; -.
DR   OrthoDB; 1605339at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0010997; F:anaphase-promoting complex binding; IEA:InterPro.
DR   GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IEA:InterPro.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR024977; Apc4-like_WD40_dom.
DR   InterPro; IPR033010; Cdc20/Fizzy.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19918; CELL DIVISION CYCLE 20 CDC20 FIZZY -RELATED; 1.
DR   PANTHER; PTHR19918:SF1; FIZZY-RELATED PROTEIN HOMOLOG; 1.
DR   Pfam; PF12894; ANAPC4_WD40; 1.
DR   Pfam; PF00400; WD40; 3.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   DOMAIN          228..303
FT                   /note="Anaphase-promoting complex subunit 4-like WD40"
FT                   /evidence="ECO:0000259|Pfam:PF12894"
FT   REPEAT          331..376
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          498..539
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          141..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   553 AA;  61245 MW;  0E049BCBEB95AB25 CRC64;
     MSSLKNSSFG KRLRASHGNG SENSPRRKRR RLDLNLDGQS SPSRSPSRRV RILAKPADVT
     NTPTRRQKVR YSSGESGDRF VPSRDRDSLK AAYSLGEQKS PSLFPKTTTR ILPDPVKDQA
     NDLYKSVLLS ELTTTTPSPG RIFAYSSPLR PRPDMSPDRF DNPTDLTYQT SPMQRETRSL
     MNQPRPHIRN IAKAPYRCLD APDLSDDFYT NLVDWSSTGI LGVGLGKSIF LWRAENQTVA
     KLCAVSDSKD EYSSVAWQRT GPTIAVGTYD GHMEIYDAST LSLIRTYKDA HNGKRIACLS
     WTADTLSSGS RDHSVQHWDH RDPSTKPFKR SVGHKQEVCG IKWSSDGGPH RALLASGGND
     NKVCVWDLRG SKRAHILGVP ELASASRALG AAATQRFTGD LPLYKFHQHK AAVKGLAWDP
     HVSGILASGG GQRDRCIRFW NTSTGTMLNE IDTGSQVCNL LWSINSHELV STHGYSTTAI
     PNQICIWKYP TMTMVSSLIG HTQCVQYVAL SPDGDSIVTG GGDQTLRFWS VFPGRTTEFK
     NEDSVLNYGK LIR
//
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